› 4al1

X-ray diffraction
1.95Å resolution

Crystal structure of Human PS-1 GSH-analog complex

Released:
DOI: 10.2210/pdb4al1/pdb
PDB 4al1 coloured by chain and viewed from the front.
PDB 4al1 coloured by chain and viewed from the side.
PDB 4al1 coloured by chain and viewed from the top.
Source organism: Homo sapiens
Entry authors: Sjogren T, Nord J, Ek M, Johansson P, Liu G, Geschwindner S

Function and Biology Details

Reactions catalysed: 
(5Z,13E)-(15S)-9-alpha,11-alpha-epidioxy-15-hydroxyprosta-5,13-dienoate = (5Z,13E)-(15S)-11-alpha,15-dihydroxy-9-oxoprosta-5,13-dienoate
RX + glutathione = HX + R-S-glutathione
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Prostaglandin E synthase Chain: A
Molecule details ›
Chain: A
Length: 152 amino acids
Theoretical weight: 17.12 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: O14684 (Residues: 1-152; Coverage: 100%)
Gene names: MGST1L1, MPGES1, PGES, PIG12, PTGES
Sequence domains: MAPEG family
Structure domains: Membrane associated eicosanoid/glutathione metabolism-like domain

Ligands and Environments


Cofactor: Ligand 48T 1 x 48T
3 bound ligands:
Ligand BOG 1 x BOG
Ligand PLM 2 x PLM
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: R3
Unit cell:
a: 76.623Å b: 76.623Å c: 123.349Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.163 0.172 0.172
Expression system: Spodoptera frugiperda

Quick links

Citations

9 review citations

Glutathionylation: a regulatory role of glutathione in physiological processes.
Dominko et al. (2018)
8 more

6 mentions without citation

Structural basis for catalysis at the membrane-water interface.
Dufrisne et al. (2017)
5 more